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B0RUZ9 (KYNU_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynU
Ordered Locus Names:xcc-b100_2707
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity. HAMAP-Rule MF_01970

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_01970

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Kynureninase HAMAP-Rule MF_01970
PRO_0000357017

Regions

Region134 – 1374Pyridoxal phosphate binding By similarity

Sites

Binding site1061Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1071Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2221Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2741Pyridoxal phosphate By similarity
Binding site3021Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RUZ9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: AAB5C7D416B3C5AF

FASTA42446,170
        10         20         30         40         50         60 
MMTDPLSRSH AAALDAADPL RALRDAFVFP QHGGQDQTYF VGNSLGLQPR QARAMVSEVL 

        70         80         90        100        110        120 
DQWGALAVEG HFTGPTQWLT YHQLVRDGLA RVVGAQPDEV VAMNTLTVNL HLMMASFYRP 

       130        140        150        160        170        180 
SAERAAILIE AGAFPSDRHA VESQLRLHGL DPDTHLIEVE PDAADGTLSM DAIAAAIAQH 

       190        200        210        220        230        240 
GPRLALVLWP GIQYRTGQAF ALGEIARLAR AQGAAVGFDL AHAVGNIPLS LHDDGVDFAV 

       250        260        270        280        290        300 
WCHYKYLNAG PGAVGGCFVH ARHAHSNLPR MAGWWGHEQP TRFRMEPQFV PSPGAEGWQL 

       310        320        330        340        350        360 
SNPPVLALAP LRASLELFDQ AGMPALRAKS EQLTGHLEQL IHTRVPQVLQ IVTPADPAQR 

       370        380        390        400        410        420 
GCQLSLRVAG GRTQGRALFE YLQSVGVLGD WREPDVIRIA PVPLYNRFCD LHQLVEHVET 


WAAA 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP52068.1.
RefSeqYP_001904112.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RUZ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_2707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP52068; CAP52068; xcc-b100_2707.
GeneID6322738.
KEGGxca:xccb100_2707.
PATRIC24085329. VBIXanCam108527_2745.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-2767-MONOMER.
UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_XANCB
AccessionPrimary (citable) accession number: B0RUZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways